Identification and Localization of Carbonic Anhydrase in Two Chlorella Species | Zendy

John R. Coleman | Zendy; Cathy Rotatore | Zendy; T. G. Williams | Zendy; Brian Colman | Zendy

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Identification and Localization of Carbonic Anhydrase in Two Chlorella Species

Author(s) -

John R. Coleman,

Cathy Rotatore,

T. G. Williams,

Brian Colman

Publication year - 1991

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.95.1.331

Subject(s) - carbonic anhydrase , extracellular , biochemistry , polyclonal antibodies , chlorella , kilodalton , biology , chlamydomonas , cytosol , chloroplast , enzyme , molecular mass , chemistry , algae , antibody , botany , mutant , gene , immunology

Carbonic anhydrase (CA) activity and localization have been examined in two species of the eukaryotic green alga Chlorella. Mass spectrometric and potentiometric assays of CA activity indicate that C. ellipsoidea contains very little extracellular CA activity whereas C. saccharophila exhibits significant extracellular activity when grown at alkaline pH values. Extracellular CA activity appears to be correlated with the presence of a 36 kilodalton polypeptide that was detected immunologically using a polyclonal antibody directed against the 37 kilodalton Chlamydomonas CA monomer. Both Chlorella species and enzymatically isolated C. ellipsoidea chloroplasts also contain an immunologically similar 38 kilodalton polypeptide that may be a cytosolic or chloroplastic form of CA.

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